Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | phosphorylation by cAMP-dependent protein kinase causes 35% inactivation of isozyme L of adipose tissue, not isozyme M | Rattus norvegicus |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
additional information | - |
additional information | - |
Rattus norvegicus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Rattus norvegicus | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
phosphoprotein | phosphorylation by cAMP-dependent protein kinase causes 35% inactivation of isozyme L of adipose tissue, not isozyme M | Rattus norvegicus |
Purification (Comment) | Organism |
---|---|
adipose tissue | Rattus norvegicus |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
ATP + beta-D-fructose 6-phosphate = ADP + beta-D-fructose 2,6-bisphosphate | bifunctional protein: 6-phosphofructo-2-kinase/fructose 2,6-bisphosphatase, reverse reaction catalysed by fructose 2,6-bisphosphatase: 3.1.3.46 | Rattus norvegicus |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
adipose tissue | equal amounts of isozyme L and M | Rattus norvegicus | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + beta-D-fructose 6-phosphate | - |
Rattus norvegicus | ADP + beta-D-fructose 2,6-bisphosphate | - |
r | |
additional information | also catalyses the degradation of fructose 2,6-bisphosphate (EC 3.1.3.46) | Rattus norvegicus | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
More | two isozymes: 55000 Da and 52000 Da | Rattus norvegicus |